(Q34909320)

English

Nucleotide binding induces changes in the oligomeric state and conformation of Sec A in a lipid environment: a small-angle neutron-scattering study

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

Nucleotide binding induces changes in the oligomeric state and conformation of Sec A in a lipid environment: a small-angle neutron-scattering study (English)

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

author name string

Zimei Bu

1

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

Ligong Wang

2

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

Debra A Kendall

3

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

language of work or name

0 references

publication date

1 September 2003

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

Journal of Molecular Biology

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

332

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

1

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

23-30

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

Complex behavior in solution of homodimeric SecA.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

The SecYEG preprotein translocation channel is a conformationally dynamic and dimeric structure

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

A dynamic model for the allosteric mechanism of GroEL

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

Evaluating the oligomeric state of SecYEG in preprotein translocase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

SecYEG assembles into a tetramer to form the active protein translocation channel

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

A method for determining transmembrane helix association and orientation in detergent micelles using small angle x-ray scattering

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

Topology of the integral membrane form of Escherichia coli SecA protein reveals multiple periplasmically exposed regions and modulation by ATP binding.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

Both an N-terminal 65-kDa domain and a C-terminal 30-kDa domain of SecA cycle into the membrane at SecYEG during translocation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

SecA of Escherichia coli traverses lipid bilayer of phospholipid vesicles.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

Two distinct ATP-binding domains are needed to promote protein export by Escherichia coli SecA ATPase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

SecYEG and SecA Are the Stoichiometric Components of Preprotein Translocase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

Specific recognition of the leader region of precursor proteins is required for the activation of translocation ATPase of Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

Complementation of two overlapping fragments of SecA, a protein translocation ATPase of Escherichia coli, allows ATP binding to its amino-terminal region

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

SecA protein needs both acidic phospholipids and SecY/E protein for functional high-affinity binding to the Escherichia coli plasma membrane

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

Characterization of membrane-associated and soluble states of SecA protein from wild-type and SecA51(TS) mutant strains of Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

Reconstitution of a protein translocation system containing purified SecY, SecE, and SecA from Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

The conformation of SecA, as revealed by its protease sensitivity, is altered upon interaction with ATP, presecretory proteins, everted membrane vesicles, and phospholipids

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

SecA, an essential component of the secretory machinery of Escherichia coli, exists as homodimer.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

8 July 2018

Phospholipid-induced monomerization and signal-peptide-induced oligomerization of SecA.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

26 October 2018

Domain interactions of the peripheral preprotein Translocase subunit SecA.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

26 October 2018

SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

26 October 2018

SecA, the peripheral subunit of the Escherichia coli precursor protein translocase, is functional as a dimer.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

26 October 2018

SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

26 October 2018

SecY, SecE, and band 1 form the membrane-embedded domain of Escherichia coli preprotein translocase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3086338

26 October 2018

SecA folds via a dimeric intermediate

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900840-4

7 January 2021

Escherichia coli SecA shape and dimensions

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900840-4

7 January 2021

Nucleotide binding activity of SecA homodimer is conformationally regulated by temperature and altered by prlD and azi mutations

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900840-4

7 January 2021

Synthetic signal peptides specifically recognize SecA and stimulate ATPase activity in the absence of preprotein

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900840-4

7 January 2021

The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900840-4

7 January 2021

UsingSitusfor the registration of protein structures with low-resolution bead models from X-ray solution scattering

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900840-4

7 January 2021

Deep penetration of a portion of Escherichia coli SecA protein into model membranes is promoted by anionic phospholipids and by partial unfolding

1 reference

https://pubmed.ncbi.nlm.nih.gov/12946344

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Reconstitution of an efficient protein translocation machinery comprising SecA and the three membrane proteins, SecY, SecE, and SecG (p12)

1 reference

https://pubmed.ncbi.nlm.nih.gov/12946344

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1016/S0022-2836(03)00840-4

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

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